SitesBLAST
Comparing WP_057506874.1 NCBI__GCF_001431535.1:WP_057506874.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
57% identity, 99% coverage: 1:578/583 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E477), G485 (= G480), R537 (= R532)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S191), Q195 (= Q193), K198 (= K196), R217 (= R215), Q226 (= Q224), F229 (= F227), Q231 (= Q229), H448 (= H443), E482 (= E477), V483 (≠ I478), G484 (= G479), G485 (= G480), G486 (= G481), R489 (= R484), L531 (≠ I526), A532 (= A527), G534 (= G529), R537 (= R532)
- binding adenosine monophosphate: F304 (= F303), V306 (= V305), K347 (= K346), G348 (= G347), A350 (= A349)
- binding : R26 (≠ V26), R28 (= R28), D29 (≠ N29), L30 (≠ Q30), G31 (= G31), S32 (≠ G32), L33 (≠ V33), F35 (= F35), Q46 (= Q46), F48 (≠ T48), D50 (≠ E50), P51 (≠ V51), R64 (≠ G64), R76 (= R76), R78 (= R78), N82 (≠ A80), N84 (= N82), M87 (= M85), E93 (= E91), P109 (= P107), D111 (≠ H109), N113 (≠ H111), H114 (≠ E112), N116 (≠ P114), T117 (≠ G115), E119 (= E117), T169 (= T167), P170 (= P168), E171 (= E169), G172 (= G170), A173 (= A171), S193 (= S191), R217 (= R215), E219 (= E217), D220 (≠ A218), R222 (= R220), A223 (= A221), R225 (= R223), I343 (≠ K342), H448 (= H443), H449 (= H444), F514 (= F509), R549 (= R544), T557 (= T552), T558 (= T553), A559 (≠ G554)
Q51422 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase; AspRS; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
56% identity, 99% coverage: 1:579/583 of query aligns to 2:585/591 of Q51422
- H31 (≠ Q30) mutation to L: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn) by 3.5-fold, by reducing enzyme's ability to misacylate tRNA(Asn) when tested against E.coli tRNA, but shows little effect when tested against P.aeruginosa tRNA.
- G82 (vs. gap) mutation to K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn) by 4.2-fold, by reducing enzyme's ability to misacylate tRNA(Asn) when tested against E.coli tRNA, but shows little effect when tested against P.aeruginosa tRNA.
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
56% identity, 99% coverage: 1:579/583 of query aligns to 1:584/585 of 4wj4A
- active site: R219 (= R215), E221 (= E217), R227 (= R223), Q228 (= Q224), E482 (= E477), G485 (= G480), R537 (= R532)
- binding aspartic acid: S195 (= S191), Q197 (= Q193), H450 (= H444), R489 (= R484), L531 (≠ I526)
- binding : R26 (≠ V26), R28 (= R28), D29 (≠ N29), H30 (≠ Q30), G31 (= G31), G32 (= G32), V33 (= V33), F35 (= F35), Q46 (= Q46), R64 (≠ G64), R76 (= R76), P79 (≠ H79), A82 (= A80), N84 (= N82), E93 (= E91), T107 (vs. gap), P109 (= P105), D113 (≠ H109), E114 (≠ A110), D117 (≠ N113), E121 (= E117), A175 (= A171), E221 (= E217), D222 (≠ A218), R224 (= R220), A225 (= A221), R227 (= R223), Y346 (= Y343), A447 (= A441), H449 (= H443), H450 (= H444), R549 (= R544), T557 (= T552), Q558 (≠ T553), S559 (≠ G554)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
56% identity, 99% coverage: 1:579/583 of query aligns to 1:584/589 of 4wj3M
- active site: R219 (= R215), E221 (= E217), R227 (= R223), Q228 (= Q224), E482 (= E477), G485 (= G480), R537 (= R532)
- binding : R28 (= R28), D29 (≠ N29), H30 (≠ Q30), G32 (= G32), V33 (= V33), F35 (= F35), Q46 (= Q46), R64 (≠ G64), R76 (= R76), R78 (= R78), A82 (= A80), N84 (= N82), E93 (= E91), T107 (vs. gap), D113 (≠ H109), V118 (≠ P114)
P56459 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase; AspRS; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
49% identity, 99% coverage: 1:579/583 of query aligns to 1:576/577 of P56459
- L81 (vs. gap) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (≠ M85) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
51% identity, 98% coverage: 1:573/583 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R215), E217 (= E217), R223 (= R223), Q224 (= Q224), E481 (= E477), G484 (= G480), R536 (= R532)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H443), D474 (= D470), E481 (= E477)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
50% identity, 99% coverage: 1:576/583 of query aligns to 2:579/580 of 4o2dA
- active site: R216 (= R215), E218 (= E217), R222 (= R223), Q223 (= Q224), E480 (= E477), G483 (= G480), R535 (= R532)
- binding aspartic acid: E170 (= E169), S192 (= S191), Q194 (= Q193), Q228 (= Q229), H446 (= H443), H447 (= H444), G483 (= G480), R487 (= R484), I529 (= I526), A530 (= A527)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
48% identity, 98% coverage: 1:573/583 of query aligns to 3:582/583 of 5w25A
- active site: R220 (= R215), E222 (= E217), R228 (= R223), Q229 (= Q224), E486 (= E477), G489 (= G480), R541 (= R532)
- binding aspartic acid: E174 (= E169), Q198 (= Q193), R220 (= R215), H452 (= H443), H453 (= H444), G489 (= G480), R493 (= R484)
- binding lysine: D159 (≠ G154), R211 (= R206)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
49% identity, 99% coverage: 2:580/583 of query aligns to 3:580/580 of 1g51B
- active site: R223 (= R215), E225 (= E217), R231 (= R223), Q232 (= Q224), E476 (= E477), G479 (= G480), R531 (= R532)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E169), S199 (= S191), Q201 (= Q193), K204 (= K196), R223 (= R215), Q232 (= Q224), F235 (= F227), Q237 (= Q229), H442 (= H443), E476 (= E477), G478 (= G479), G479 (= G480), G480 (= G481), R483 (= R484), I525 (= I526), A526 (= A527), G528 (= G529), R531 (= R532)
- binding adenosine monophosphate: V313 (= V305), Q347 (≠ K346), G348 (= G347), L349 (= L348), A350 (= A349), V389 (≠ G390), A390 (= A391)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
49% identity, 99% coverage: 2:580/583 of query aligns to 3:580/580 of 1g51A
- active site: R223 (= R215), E225 (= E217), R231 (= R223), Q232 (= Q224), E476 (= E477), G479 (= G480), R531 (= R532)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E169), Q201 (= Q193), K204 (= K196), R223 (= R215), R231 (= R223), Q232 (= Q224), F235 (= F227), Q237 (= Q229), H442 (= H443), H443 (= H444), E476 (= E477), G478 (= G479), G479 (= G480), G480 (= G481), R483 (= R484), I525 (= I526), A526 (= A527), G528 (= G529), R531 (= R532)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
49% identity, 99% coverage: 2:580/583 of query aligns to 3:580/580 of 1efwA
- active site: R223 (= R215), E225 (= E217), R231 (= R223), Q232 (= Q224), E476 (= E477), G479 (= G480), R531 (= R532)
- binding : R27 (≠ V26), R29 (= R28), D30 (≠ N29), L31 (≠ Q30), G32 (= G31), G33 (= G32), L34 (≠ V33), F36 (= F35), Q47 (= Q46), H51 (≠ E50), P52 (≠ D52), R64 (≠ G64), R78 (= R78), E80 (≠ A80), N82 (= N82), R84 (≠ K84), E91 (= E91), T105 (≠ P105), P107 (= P107), E125 (= E117), R343 (≠ K342)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
49% identity, 99% coverage: 2:580/583 of query aligns to 4:581/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E169), Q202 (= Q193), K205 (= K196), R224 (= R215), R232 (= R223), Q233 (= Q224), F236 (= F227), Q238 (= Q229), E477 (= E477), V478 (≠ I478), G479 (= G479), G480 (= G480), G481 (= G481), R484 (= R484), I526 (= I526), A527 (= A527), G529 (= G529), R532 (= R532)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
49% identity, 99% coverage: 2:578/583 of query aligns to 4:573/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q193), K205 (= K196), R224 (= R215), F236 (= F227), Q238 (= Q229), H438 (= H443), E472 (= E477), V473 (≠ I478), G474 (= G479), G475 (= G480), G476 (= G481), R479 (= R484), I521 (= I526), A522 (= A527), G524 (= G529)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
49% identity, 99% coverage: 2:578/583 of query aligns to 4:573/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q193), K205 (= K196), R224 (= R215), F236 (= F227), Q238 (= Q229), H438 (= H443), E472 (= E477), V473 (≠ I478), G474 (= G479), G475 (= G480), G476 (= G481), R479 (= R484), I521 (= I526), A522 (= A527), G524 (= G529)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
49% identity, 99% coverage: 2:578/583 of query aligns to 4:573/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q193), R224 (= R215), F236 (= F227), Q238 (= Q229), H438 (= H443), E472 (= E477), V473 (≠ I478), G474 (= G479), G475 (= G480), G476 (= G481), R479 (= R484), I521 (= I526), A522 (= A527), G524 (= G529), R527 (= R532)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
49% identity, 99% coverage: 2:578/583 of query aligns to 4:572/573 of 7ap4A
- binding (3~{S})-3-azanyl-4-[[(2~{R},3~{S},4~{R},5~{R})-5-[7-azanyl-5-(hydroxymethyl)benzimidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxysulfonylamino]-4-oxidanylidene-butanoic acid: Q200 (= Q193), R222 (= R215), R230 (= R223), Q231 (= Q224), F234 (= F227), Q236 (= Q229), E471 (= E477), G473 (= G479), G474 (= G480), G475 (= G481), R478 (= R484), I520 (= I526), A521 (= A527), G523 (= G529)
4o2dB Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
46% identity, 99% coverage: 1:576/583 of query aligns to 2:514/515 of 4o2dB
- active site: R216 (= R215), E218 (= E217), R222 (= R223), Q223 (= Q224), E415 (= E477), G418 (= G480), R470 (= R532)
- binding aspartic acid: E170 (= E169), S192 (= S191), Q194 (= Q193), Q228 (= Q229), H382 (= H444), G418 (= G480), R422 (= R484), I464 (= I526), A465 (= A527)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
41% identity, 99% coverage: 1:578/583 of query aligns to 49:633/645 of Q6PI48
- R58 (≠ D10) mutation to G: No effect on its mitochondria localization.
- T136 (= T87) mutation to S: No effect on its mitochondria localization.
- Q184 (= Q133) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (= R212) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ A288) mutation to E: No effect on its mitochondria localization.
- L613 (= L558) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L571) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918213
Sites not aligning to the query:
- 45 S → G: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918209
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
35% identity, 48% coverage: 2:279/583 of query aligns to 3:293/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
35% identity, 48% coverage: 2:279/583 of query aligns to 3:293/438 of 3nemA
Sites not aligning to the query:
- active site: 361, 364, 412
- binding aspartyl-adenosine-5'-monophosphate: 339, 361, 362, 363, 364, 365, 368, 406, 407, 409, 412
Query Sequence
>WP_057506874.1 NCBI__GCF_001431535.1:WP_057506874.1
MRTHFCGLVDETLIGQTVTLAGWTDVARNQGGVCFIDLRDHEGIVQVTVEVDNAEVFAVA
ASLGYEDVLQVEGVVRARHAVNDKMATGKVEVIATAITVLNKAAPLPFHAHENPGEETRL
KYRYLDLRRPEMQRMQRTRIKLVQALRRHLDERGFQDIETPILTKATPEGARDFLVPARM
HPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVREQ
DVQDFVEDMIRGIFKEVVDVELDARFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKS
SEFPVFTAAANDADGRVAALRIPGGATLSRKQIDEYAAHAAKYGAKGLAYIKVGENGEIS
SPIQKFFSEDGFAALLAHVGAGKGDIVFFGAGGYNKVSDFMGALRLKAGKDFGLVADGWA
PLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRTHAKTAVSRGYDMVLNGNEIGG
GSIRIHRPDMQSAVFELLGIDAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGT
ESIRDVIPFPKTTGAQCLMTDAPSPIADAQLAEVHIQVRPKKA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory